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1 t two of the five cysteine residues in human glutaredoxin.
2 nzymes such as glutathione S-transferase and glutaredoxin.
3 from immobilized S-glutathionylated actin to glutaredoxin.
4 the reactivation of RNR through reduction of glutaredoxins.
5 isulfide on par with mammalian and bacterial glutaredoxins.
6 es required for synthesis of glutathione and glutaredoxins.
7 cystine reductase activity characteristic of glutaredoxins.
8 member of this new expanding family of large glutaredoxins.
9 lications for protein disulfide reduction by glutaredoxins.
10  reducing proteins glutaredoxin 3 (Grx3) and glutaredoxin 1 (Grx1) are structurally similar but exhib
11 hione redox couple: Inhibition of endogenous glutaredoxin 1 (Grx1) disrupted roGFP2 responses to O(3)
12                                              Glutaredoxin 1 (Grx1) is an evolutionally conserved anti
13                   Here we report the role of glutaredoxin 1 (Grx1), an antioxidant enzyme, in flow-me
14           Moreover, neutrophils deficient in glutaredoxin 1 (Grx1), an enzyme required for deglutathi
15                                Disruption of glutaredoxin 1 (Grx1), an enzyme that catalyzes actin de
16            Glutathionylation was reversed by glutaredoxin 1 (Grx1), and GSH plus Grx1 was able to sup
17  green fluorescent protein 2, coupled to the glutaredoxin 1 (Grx1-roGFP2).
18   Strains that lack thioredoxins 1 and 2 and glutaredoxin 1 do not grow because RNR remains in its ox
19 storing the ability of Atox1 to bind copper; glutaredoxin 1 facilitates this reaction when GSH is low
20 eak Na(+)-K(+) pump current when we included glutaredoxin 1 in patch pipette solutions to reverse glu
21 lically stressed monocytes by overexpressing glutaredoxin 1 protected MKP-1 from degradation and norm
22              This reaction was stimulated by glutaredoxin 1 via the so-called monothiol mechanism.
23 G, proline increased the expression of grxA (glutaredoxin 1) and trxC (thioredoxin 2) of the OxyR reg
24 edoxin superfamily, thioredoxins 1 and 2 and glutaredoxin 1, is unable to grow, a phenotype presumed
25 o that its properties are closer to those of glutaredoxin 1.
26                                              Glutaredoxin-1 (Glrx) is a cytosolic enzyme that regulat
27                                              Glutaredoxin-1 (Glrx) is a small cytosolic enzyme that r
28                              AAVs coding for glutaredoxin-1 (Glrx) shRNA successfully inhibited Glrx
29  reversed by the cytosolic thioltransferase, glutaredoxin-1 (Glrx).
30 hionylation, that are selectively removed by glutaredoxin-1 (Glrx).
31  in lungs of mice lacking and overexpressing glutaredoxin-1 (Glrx1), and wild-type (WT) mice in respo
32 and the specific deglutathionylation reagent glutaredoxin-1 (Grx1).
33 n of Fas (Fas-SSG), which can be reversed by glutaredoxin-1 (Grx1).
34                   Recently, the human enzyme glutaredoxin-1 (hGrx1) has been shown to possess Cu meta
35  catalase, a dominant-negative p47(phox), or glutaredoxin-1 decreased GSS-Ras, Ras activation, p38, a
36 promotes clearance of P. aeruginosa and that glutaredoxin-1 impairs bacterial clearance and increases
37                                              Glutaredoxin-1 overexpression maintained endogenous SirT
38 n of SERCA, and adenoviral overexpression of glutaredoxin-1 prevented both the HNO-stimulated oxidati
39 PTMs of SirT1 are glutathione (GSH) adducts, glutaredoxin-1 was overexpressed to remove this modifica
40 ss spectroscopy, five proteins, cathepsin G, glutaredoxin-1, thioredoxin, GP1b, and fibrinogen, showe
41                            E. coli has three glutaredoxins: 1, 2, and 3, each with a classical -Cys-P
42                                              Glutaredoxin 2 (Grx2) from Escherichia coli is distingui
43                          Vertebrate-specific glutaredoxin 2 (Grx2) is expressed in at least two isofo
44 Here, we discovered an essential function of glutaredoxin 2 during vascular development.
45              Consequently, overexpression of glutaredoxin 2 in the IMS results in a more reduced Mia4
46  revealed that morpholino-based knockdown of glutaredoxin 2 in zebrafish, a model organism to study v
47                               In this report glutaredoxin 2 is shown to be the most effective hydroge
48 umed common ancestor of cytosolic GSTs (i.e. glutaredoxin 2).
49 ryogenesis has recently been exemplified for glutaredoxin 2, a vertebrate-specific glutathione-disulf
50 ion of a functional vascular system requires glutaredoxin 2-dependent reversible S-glutathionylation
51                                     Thereby, glutaredoxin 2-mediated redox regulation controls enzyma
52  catalytic region of sirtuin 1 as target for glutaredoxin 2-specific deglutathionylation.
53                                              Glutaredoxin-2 (Grx2) modulates the activity of several
54                    Here, we demonstrate that glutaredoxin-2 (Grx2), a matrix oxidoreductase, is requi
55                        The reducing proteins glutaredoxin 3 (Grx3) and glutaredoxin 1 (Grx1) are stru
56 s dependent on the action of a host protein, glutaredoxin 3 (GrxC).
57                    Furthermore, we show that glutaredoxin 3 requires the glutathione biosynthesis pat
58 ion of mutations in the gene for the protein glutaredoxin 3 that suppress the growth defect.
59 ations that lead to RNR overproduction allow glutaredoxin 3 to reduce sufficient RNR for growth of th
60  cell allows more effective interaction with glutaredoxin 3, thus restoring an effective pool of deox
61                    Human cytosolic monothiol glutaredoxin-3 (GLRX3) is a protein essential for the ma
62 tional role of the interaction between human glutaredoxin-3 (GRX3) and its protein partner BOLA2, we
63  [2Fe-2S]-bridged heterodimer formed between glutaredoxin-3 and the BolA-like protein Fe repressor of
64                                              Glutaredoxin 5 (GLRX5) deficiency has previously been id
65 racterization tool is demonstrated with holo glutaredoxin 5 (GLRX5) homodimer and holo GLRX5:BolA-lik
66                                Together with glutaredoxin 5 (GLRX5), HSCB and HSPA9 facilitate the tr
67 LIAS), BolA type 3 (BOLA3), and a novel gene glutaredoxin 5 (GLRX5).
68  that Ssq1 also interacts with the monothiol glutaredoxin 5 (Grx5) at a binding site different from t
69                    In mitochondria monothiol glutaredoxin 5 (GRX5) is involved in the maturation of a
70       Saccharomyces cerevisiae mitochondrial glutaredoxin 5 (Grx5) is the archetypical member of a ub
71 zebrafish mutants is caused by deficiency of glutaredoxin 5 (grx5), a gene required in yeast for Fe-S
72 de a sideroblastic anemia with deficiency of glutaredoxin 5 and a myopathy associated with a deficien
73 ever, the human diseases, Friedreich ataxia, glutaredoxin 5-deficient sideroblastic anemia, ISCU myop
74                                              Glutaredoxin 6 (Grx6) of Saccharomyces cerevisiae is an
75 eved with the reduced form of glutathione or glutaredoxin, a protein known to replace thioredoxin in
76                         Both lipoic acid and glutaredoxins act in the reverse manner from their norma
77 een the toxin sulfurs and cysteine 22 in the glutaredoxin active site.
78         Purified recombinant Pv5-6 exhibited glutaredoxin activity that was increased 1.6-fold by 10
79 ng (13)C-labeled glucose, and an increase in glutaredoxin activity, which catalyzes the glutathione-d
80 sults reveal a novel neuroprotective role of glutaredoxin against dopaminergic neurodegeneration in m
81                Proteins such as thioredoxin, glutaredoxin, albumin, beta-lactoglobulin, and lactopero
82 ndings thus indicate that carefully balanced glutaredoxin amounts in the IMS ensure efficient oxidati
83  balance between cellular reductants such as glutaredoxin and copper activation pathways in controlli
84 ese results present a physiological role for glutaredoxin and ROS- induced reversible actin glutathio
85 ow that H encodes a novel epidermis-specific glutaredoxin and that the pattern of trichome distributi
86         In Escherichia coli, the glutathione/glutaredoxin and thioredoxin pathways are essential for
87     Using these proteins, we showed that the glutaredoxin and thioredoxin reductase domains of TGR co
88       Reduction of Hsp33 is catalyzed by the glutaredoxin and thioredoxin systems in vivo, and leads
89 redox homeostasis, including the glutathione/glutaredoxin and thioredoxin systems.
90  cross talk existing between the glutathione/glutaredoxin and Trx-dependent pathways.
91                      The interaction between glutaredoxins and Aft1 is not modulated by the iron stat
92           In particular, cytosolic monothiol glutaredoxins and BolA-like proteins have been identifie
93 h a high amino acid sequence similarity with glutaredoxins and mycoredoxins but with a thioredoxin-li
94                                              Glutaredoxins and thioredoxins are highly conserved, sma
95                                              Glutaredoxins and thioredoxins are ubiquitous small heat
96 ative participation of the thioltransferase (glutaredoxin) and thioredoxin systems in overall cellula
97 S] clusters on Rieske, ferredoxin (Fdx), and glutaredoxin), and cluster oxidation states.
98 including glucanase, glutathione peroxidase, glutaredoxin, and a profilin were found to be widely exp
99 lular thiol oxidoreductases, thioredoxin and glutaredoxin, and found that these enzymes can control t
100      Glutathione S-transferase, thioredoxin, glutaredoxins, and DNA repair enzymes responded most str
101 d enzymes, including glutathione reductases, glutaredoxins, and glutathione S-transferases, indicated
102  we conclude that catalase and peroxiredoxin-glutaredoxin are determinants of bacterial persistence d
103 E10R and L1R viral membrane proteins and the glutaredoxin are in the cytoplasm, in which assembly of
104 stically in fungi and higher eukaryotes, the glutaredoxins are conserved, yet their precise function
105          In yeast cells, cytosolic monothiol glutaredoxins are required for the formation of heme and
106 zing glutathione as a resolving cysteine and glutaredoxin as a redox partner.
107 ction of arsenate to arsenite using GSH with glutaredoxin as electron donors.
108            rSynArsC employed glutathione and glutaredoxin as the source of reducing equivalents, like
109                    Activity required GSH and glutaredoxin as the source of reducing equivalents.
110 we demonstrate that an Arabidopsis monothiol glutaredoxin, AtGRXS17 (At4g04950), plays a critical rol
111 ich has a redox potential similar to that of glutaredoxin, becomes essential for cell survival when G
112 se, superoxide dismutases, thioredoxins, and glutaredoxins between normal Prdx6-/- and Prdx6+/+ mice
113 po-form of A4V SOD1 was highly reactive with glutaredoxin but not SOD1 containing both copper and zin
114 isulfides, containing one adducted toxin per glutaredoxin but with elimination of two sulfur atoms fr
115 Escherichia coli is distinguished from other glutaredoxins by its larger size, low overall sequence i
116                                 We find that glutaredoxins can promote disulfide bond formation in th
117 subclass of the thioredoxin superfamily, the glutaredoxins, can become disulfide bond-formation catal
118 g to Grx1(as) cDNA showed that two different glutaredoxin cDNAs (Grx1(as) and Grx1) were generated fr
119 es within the DsbA family different from the glutaredoxin cluster to which mycoredoxin-1 (Mrx1 or Rv3
120        GRXS17 is a nucleocytosolic monothiol glutaredoxin consisting of an N-terminal thioredoxin dom
121       The glutaredoxin domain is a monothiol glutaredoxin containing a CxxS motif at the active site,
122 e observed that the catalytic enhancement by glutaredoxin could be ascribed fully to the difference b
123                              The inactivated glutaredoxin could be reactivated by dithiothreitol only
124  concentration of inducer, and the amount of glutaredoxin could be varied from barely detectable to g
125   Physiological reductases, thioredoxins and glutaredoxins, could not dissolve AtGAPC1 aggregates but
126 ave identified mutations in the gene Grxcr1 (glutaredoxin cysteine-rich 1) in five independent alleli
127 nt in GSH biosynthesis) that is defective in glutaredoxin-dependent redox signaling and ntra/ntrb (de
128 ly complex proteins or deletion of cytosolic glutaredoxins did not reduce expression of Yap5 target g
129 or of thioredoxin 1 in this environment, the glutaredoxins do so independently of DsbB.
130 edoxin reductases, it contains an N-terminal glutaredoxin domain and exhibits a wide spectrum of enzy
131                         It has an additional glutaredoxin domain and shows highest expression in test
132 entified, which is a fusion of an N-terminal glutaredoxin domain and the TR module.
133 s of cells but is dependent on the conserved glutaredoxin domain Cys residue.
134                                          The glutaredoxin domain is a monothiol glutaredoxin containi
135 ged between a BOLA2 molecule and a monothiol glutaredoxin domain of GRX3, and to transfer both [2Fe-2
136 de center within the TR domain to either the glutaredoxin domain or Trx.
137 to 72 forming a classical "thioredoxin-fold" glutaredoxin domain, connected by an 11 residue linker t
138 ch is v3 that carries an atypical N-terminal glutaredoxin domain.
139 he thiol/disulfide active site of TGR to the glutaredoxin domain.
140  evolutionary conserved fusion of the TR and glutaredoxin domains.
141 ox pathway was found for O2L, a nonessential glutaredoxin encoded by vaccinia virus.
142 ed by hktE) and a bifunctional peroxiredoxin-glutaredoxin (encoded by pdgX) in resistance of NTHI to
143  catalase-peroxidase system, but thioredoxin/glutaredoxin enzymes might alleviate oxidative stress.
144 Importantly, treatment of inactive KGDH with glutaredoxin facilitated the GSH-dependent recovery of K
145 interaction between members of the monothiol glutaredoxin family and members of the BolA-like protein
146 ld type highlights the role of mitochondrial glutaredoxin Fe-S-binding in whole plant growth and toxi
147                                     However, glutaredoxins from both S. cerevisiae and E. coli were a
148 signaling and that cytokinins could activate glutaredoxin gene expression independent of plant nitrat
149      We determined that nitrate induction of glutaredoxin gene expression was dependent upon cytokini
150 h2 mutation was caused by transposition of a glutaredoxin gene, MALE STERILE CONVERTED ANTHER1 (MSCA1
151               RNA silencing of four of these glutaredoxin genes (AtGRXS3/4/5/8) resulted in plants wi
152 dox state of the cell, particularly a set of glutaredoxin genes.
153                                The monothiol glutaredoxin Glrx3 and BolA2 function as a [2Fe-2S] chap
154 se clusters are transferred to the monothiol glutaredoxin GLRX5 by an Hsp70 system followed by insert
155  substrates are protein disulfide isomerase, glutaredoxin, glutathione peroxidase, NK-lysin/granulysi
156    Thus, thioredoxin was more efficient than glutaredoxin, glutathione, or a 14-kDa thioredoxin-like
157                                              Glutaredoxin (Grx) and protein-disulfide isomerase (PDI)
158 as composed of a basic TR1 module fused to a glutaredoxin (Grx) domain that contained an unusual acti
159                                              Glutaredoxin (Grx) is a ubiquitous redox molecule that i
160 tion of deoxyribonucleotides are provided by glutaredoxin (Grx) or thioredoxin (Trx).
161 nhibitory RNA (siRNA) directed against GR or glutaredoxin (Grx) potentiated adriamycin-induced macrop
162 mulator fern Pteris vittata L., a cDNA for a glutaredoxin (Grx) Pv5-6 was isolated from a frond expre
163        Redox molecules thioredoxin (Trx) and glutaredoxin (Grx) superfamilies actively maintain intra
164                        Thioredoxin (Trx) and glutaredoxin (Grx) systems have been implicated as elect
165                                              Glutaredoxin (Grx) was deactivated in a dose-dependent f
166                               Epitope-tagged glutaredoxin (GRX) was utilized to determine the role of
167                                        Human glutaredoxin (GRx), also known as thioltransferase, is a
168  oxidoreductase component of the GSH system, glutaredoxin (Grx), is involved in the reduction of GSH-
169 onylation of IKK-beta Cys-179 is reversed by glutaredoxin (GRX), which restores kinase activity.
170                                              Glutaredoxin (GRx), which specifically catalyzes reducti
171                                              Glutaredoxin (Grx)-catalyzed deglutathionylation of prot
172 uction of AR-SSG to AR-SH was facilitated by glutaredoxin (GRX).
173                                              Glutaredoxin (GRx, thioltransferase) is implicated in ce
174 is catalyzed specifically and efficiently by glutaredoxin (GRx, thioltransferase), a thioldisulfide o
175 ard mixed disulfides between glutathione and glutaredoxin (Grx-S-SG), consistent with the in vivo req
176              The yeast monothiol multidomain glutaredoxins (Grx) 3 and 4 are essential for both trans
177 edox) changes in the glutathione pool (GSH), glutaredoxins (GRX) and thioredoxins (TRX) are important
178 ns of oxidative stress and are controlled by glutaredoxins (Grx) that, under physiological conditions
179 (1) Several recent reports have demonstrated glutaredoxins (Grx) to form [Fe(2)S(2)] cluster-bridged
180 [2Fe-2S]-containing complexes with monothiol glutaredoxins (Grx), structural details are lacking.
181                  Alternatively spliced human glutaredoxin (Grx1(as)) cDNA was isolated from a neutrop
182 il cDNA library, using a (32)P-labeled human glutaredoxin (Grx1) cDNA probe under non-stringent condi
183 frame of the previously reported first human glutaredoxin (Grx1) cDNA, but the 3'-untranslated region
184                                              Glutaredoxin (Grx1) plays a key role in such regulation
185 contains two gene pairs encoding cytoplasmic glutaredoxins (GRX1, GRX2) and thioredoxins (TRX1, TRX2)
186 the form of [2Fe-2S]-GSH2 from the monothiol glutaredoxin Grx3/4, and the same electron source, in th
187 We presently show that the nuclear monothiol glutaredoxins Grx3 and Grx4 are critical for iron inhibi
188 A homologue Fra2 and the cytosolic monothiol glutaredoxins Grx3 and Grx4 together play a key role in
189  likely dependent on the cytosolic monothiol glutaredoxins Grx3/Grx4 and the Fe-S cluster protein Dre
190 athway that includes the cytosolic monothiol glutaredoxins (Grx3 and Grx4) and the BolA homologue Fra
191 NG1 to suppress disease susceptibility genes glutaredoxins GRX480, GRXS13 and thioredoxin TRX-h5.
192 3 form dimeric complexes with both monothiol glutaredoxin Grx5 and Nfu1.
193 on-sulfur cluster formation on the monothiol glutaredoxin (GRX5) acceptor protein.
194 arlier in Fe-S biogenesis with the monothiol glutaredoxin, Grx5, and Bol3 functions late with Nfu1.
195 roteins, accessory factors such as monothiol glutaredoxin, GrxD, and the FeS carrier protein NfuA are
196 structural similarity, CxxC/S-type (class I) glutaredoxins (Grxs) act as oxidoreductases, while CGFS-
197                          Cytosolic monothiol glutaredoxins (GRXs) are required in iron-sulfur (Fe-S)
198                                              Glutaredoxins (Grxs) are small oxidoreductases that redu
199                                              Glutaredoxins (Grxs) are small proteins that function as
200                                              Glutaredoxins (Grxs) are ubiquitous small heat-stable di
201                                              Glutaredoxins (GRXs) catalyze the reduction of protein d
202                                              Glutaredoxins (GRXs) modulate redox-dependent signaling
203 idative modification that can be reversed by glutaredoxins (Grxs).
204 using T(SH)(2) instead of GSH, including the glutaredoxins (Grxs).
205        Here, we examined the function of the glutaredoxin GRXS17, a member of thiol reductase familie
206 ete reactivation was only possible using the glutaredoxin/GSH system (97 +/- 4% and 91 +/- 3% for hBC
207                    We concluded that the two glutaredoxin homologs encoded by vaccinia virus have dif
208 ioned in two activities that are typical for glutaredoxins, hydroxyethyl disulfide reduction and elec
209 ed Srx as the reaction intermediate, whereas glutaredoxin I was more favorable for deglutathionylatin
210                     Furthermore, relative to glutaredoxin I, Srx exhibited negligible deglutathionyla
211  current study sporidesmin inactivated human glutaredoxin in a time- and concentration-dependent mann
212 scU to apo-Grx5, a general purpose monothiol glutaredoxin in A. vinelandii, was monitored by circular
213 recedented role for the thiol oxidoreductase glutaredoxin in reducing the SOD1 disulfide and destabil
214  These data suggest that redox regulation by glutaredoxin in retinal glial cells is perturbed by hype
215 rved role of cytosolic monothiol multidomain glutaredoxins in cellular iron metabolism pathways, incl
216 ristem size and revealed a novel function of glutaredoxins in meristem growth.
217          Here we demonstrate the presence of glutaredoxins in the IMS and show that limiting amounts
218 ds to Grx3 and Grx4, two cytosolic monothiol glutaredoxins, in an iron-independent fashion.
219 epidithiopiperazine-2,5-diones to inactivate glutaredoxin indicated that at least one phenyl substitu
220 ubstitutions in the active site of the three glutaredoxins indicated that only the N-terminal cystein
221 specific dethiolase enzyme thioltransferase (glutaredoxin), indicating that the inactivated form of t
222 tranferase), because Cd(II), an inhibitor of glutaredoxin, inhibits intracellular actin deglutathiony
223 s of the oxidized probe with glutathione and glutaredoxin into a larger kinetic model of peroxide met
224                                              Glutaredoxin is characterized as a specific and efficien
225 disulfide interchange; either thioredoxin or glutaredoxin is then thought to reduce the cystine that
226   The primary function of Grx2 as a GST-like glutaredoxin is to catalyze reversible glutathionylation
227 art of the conserved CGFS motif in monothiol glutaredoxins is essential for this function.
228 n S-glutathionylation, and thioltransferase (glutaredoxin) is a specific and efficient catalyst of pr
229         Cp9 (a distant relative of bacterial glutaredoxins) is a direct electron acceptor for Cp34, p
230                               By using these glutaredoxin knocked-out cells, we have demonstrated tha
231 ion, indicating that the protein possesses a glutaredoxin-like activity.
232 APR) is composed of a reductase domain and a glutaredoxin-like C-terminal domain.
233 lines with the attB site integrated into the glutaredoxin-like cg6 gene.
234 bolism encode a second thioredoxin (TrxC), a glutaredoxin-like protein and enzymes involved in the bi
235 as thioredoxins, thioredoxin reductases, and glutaredoxin-like proteins.
236  potential thioredoxin reductases, and three glutaredoxin-like proteins.
237 a and beta subunits of RNR; NrdH and TrxR, a glutaredoxin-like thioredoxin and a thioredoxin reductas
238                                    MtMrx1, a glutaredoxin-like, mycothiol-dependent oxidoreductase, d
239                        Glutathione-dependent glutaredoxin-mediated deglutathionylation of eNOS has be
240              We hypothesized that changes in glutaredoxin might be important in the development of di
241                            With this method, glutaredoxin, monitored by Western blot, was knocked out
242                                    Monothiol glutaredoxins (mono-Grx) represent a highly evolutionari
243                   Vaccinia virus encodes two glutaredoxins, O2L and G4L, both of which exhibit thiolt
244            Specifically, the major cytosolic glutaredoxin of yeast was seen to reduce the intramolecu
245 ionylation of the alpha subunit catalyzed by glutaredoxin or dithiothreitol resulted in restoration o
246 by PrxV is reduced by thioredoxin but not by glutaredoxin or glutathione.
247 as reductant directly in the active site, or glutaredoxins or thioredoxins reduce a C-terminal cystei
248 t of the system revealed no interaction with glutaredoxins or thioredoxins, indicating that this clas
249 lar thiol oxidoreductases that interact with glutaredoxins or thioredoxins.
250 ion are delivered by a redoxin (thioredoxin, glutaredoxin, or NrdH) via a pair of conserved active si
251  the single-cysteine omega class, which have glutaredoxin oxidoreductase activity rather than GSH-S-t
252 due to their capacity to tap the glutathione/glutaredoxin pathway for DNA biosynthesis.
253 uctase, AhpC*, active in the glutathione and glutaredoxin pathway.
254 ced state by the thioredoxin and glutathione/glutaredoxin pathways.
255 selen known to modulate both thioredoxin and glutaredoxin pathways.
256 These include catalase (HktE), peroxiredoxin/glutaredoxin (PgdX), and a ferritin-like protein (Dps).
257                                    Monothiol glutaredoxins play a crucial role in iron-sulfur (Fe/S)
258 olds have diverged from a common thioredoxin/glutaredoxin progenitor but did so by different mechanis
259 tein that contains a region of similarity to glutaredoxin proteins and a cysteine-rich region at its
260  IMS and show that limiting amounts of these glutaredoxins provide a kinetic barrier to prevent the t
261 of the Grx1(as) genomic gene, two additional glutaredoxin pseudogenes were also isolated.
262 owing that a poplar ortholog is reduced by a glutaredoxin rather than NADP-thioredoxin reductase.
263 d (glutathione S-transferase P) and reverse (glutaredoxin) reactions creates a functional cycle that
264 n Bacteroides fragilis lacks the glutathione/glutaredoxin redox system and possesses an extensive num
265                              Thioredoxin and glutaredoxin reduce the oxidized Dio3 at physiological c
266 e functionally replaces glutathione, and the glutaredoxins replace LpdA.
267                              Inactivation of glutaredoxin required the reduced (dithiol) form of the
268 ally characterized the role of mitochondrial glutaredoxin S15 (GRXS15) in biogenesis of ISC containin
269                           Cells lacking both glutaredoxins show constitutive expression of iron regul
270 " cytokinin-deficient plants and "long-root" glutaredoxin-silenced plants generated hybrids that disp
271 se has been shown to require glutathione and glutaredoxin, suggesting that thiol chemistry might be i
272                           In conclusion, the glutaredoxin system and glutathione have a backup role t
273 utants lacking components of the glutathione/glutaredoxin system are unaffected.
274 e redox Western blot data indicated that the glutaredoxin system protected Trx1 in HeLa cells from ox
275 lutathionylation of hBCATc-SSG using the GSH/glutaredoxin system provides evidence that this protein
276 ts strongly suggest that the thioredoxin and glutaredoxin systems are the key regulators for hSOD1 ag
277 uctase (TryR) instead of the thioredoxin and glutaredoxin systems of mammalian hosts.
278 reased the capability of the thioredoxin and glutaredoxin systems to reduce hSOD1 compared with wild-
279  The carboxyl-terminal domain functions as a glutaredoxin that mediates the transfer of electrons fro
280 of intramolecular disulfide bonds of the G4L glutaredoxin, the L1R membrane protein, and the structur
281                                              Glutaredoxin therefore preferentially targets the immatu
282 lutathionylation is most likely catalyzed by glutaredoxin (thioltranferase), because Cd(II), an inhib
283                                              Glutaredoxin (thioltransferase) is a thiol-disulfide oxi
284 osphatases using a descriptor built from the glutaredoxin/thioredoxin family, proteins that have no a
285 iosynthetic enzymes, glutathione reductases, glutaredoxins, thioredoxins, and thioredoxin reductases,
286 d disulfide with GSH before being reduced by glutaredoxin to regenerate the active Acr2p reductase.
287 d disulfide with GSH before being reduced by glutaredoxin to regenerate the active ArsC reductase.
288 e active RNR, the cell uses thioredoxins and glutaredoxins to reduce the disulfide bond.
289  of [2Fe-2S] cluster transfer from monothiol glutaredoxins to target proteins is a fundamental, but s
290  Aspartic proteases, BTB/POZ proteins (BTB), Glutaredoxins, Trypsin alpha-amylase inhibitor proteins,
291 n-associated protein, focal adhesion kinase, glutaredoxin, utrophin) may be novel mediators of NFT fo
292                               By comparison, glutaredoxin was less reactive toward the disulfide of w
293        Various cysteine-to-serine mutants of glutaredoxin were resistant to inactivation by sporidesm
294               Seven genes encoding class III glutaredoxins were found to be strongly and specifically
295 namely, the L1R and F9L proteins and the G4L glutaredoxin-were completely reduced.
296 iamide-GSH is partially recovered by DTT and glutaredoxin, whereas the disulfide linkage of GSH with
297 ytosolic compartment that involves monothiol glutaredoxins, which bind iron in the form of iron-sulfu
298 al member of a ubiquitous class of monothiol glutaredoxins with a strictly conserved CGFS active-site
299 th the help of thioredoxin reductase and the glutaredoxins with the small molecule glutathione and gl
300  pathways via either the thioredoxins or the glutaredoxins without, evidently, the intermediary of gl

 
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